Effect of High Hydrostatic Pressure Intensity on Structural Modifications in Mealworm (Tenebrio molitor) Proteins
Bibliographic record
Abstract
Processing edible insects into protein extracts may improve consumer acceptability. However, a better understanding of the effects of food processing on the proteins is needed to facilitate their incorporation into food matrices. In this study, soluble proteins from Tenebrio molitor (10% w/v) were pressurized using high hydrostatic pressure (HHP) at 70–600 MPa for 5 min and compared to a non-pressurized control (0.1 MPa). Protein structural modifications were evaluated using turbidity measurement, particle-size distribution, intrinsic fluorescence, surface hydrophobicity, gel electrophoresis coupled with mass spectrometry, and transmission electron microscopy (TEM). The observed decrease in fluorescence intensity, shift in the maximum emission wavelength, and increase in surface hydrophobicity reflected the unfolding of mealworm proteins. The formation of large protein aggregates consisting mainly of hexamerin 2 and ⍺-amylase were confirmed by protein profiles on gel electrophoresis, dynamic light scattering, and TEM analysis. The typical aggregate shape and network observed by TEM after pressurization indicated the potential involvement of myosin and actin in aggregate formation, and these were detected by mass spectrometry. For the first time, the identification of mealworm proteins involved in protein aggregation phenomena under HHP was documented. This work is the first step in understanding the mealworm protein–protein interactions necessary for the development of innovative insect-based ingredients in food formulations.
Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.
How this classification was reachedexpand
Full frame machine prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.
Distilled classifier scores by category (both heads)
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.000 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.001 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from itClassification
machine, unvalidatedMachine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.
How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".